Solid-state NMR sequential assignment of the β-endorphin peptide in its amyloid form

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• 作者：Carolin Seuring ; Julia Gath ; Joeri Verasdonck…
• 关键词：β ; endorphin fibrils ; Functional amyloid ; Solid ; state NMR ; Assignment ; Secondary structure ; β ; strand
• 刊名：Biomolecular NMR Assignments
• 出版年：2016
• 出版时间：October 2016
• 年：2016
• 卷：10
• 期：2
• 页码：259-268
• 全文大小：3,703 KB
• 刊物类别：Physics and Astronomy
• 刊物主题：None Assigned
• 出版者：Springer Netherlands
• ISSN：1874-270X
• 卷排序：10

文摘

Insights into the three-dimensional structure of hormone fibrils are crucial for a detailed understanding of how an amyloid structure allows the storage of hormones in secretory vesicles prior to hormone secretion into the blood stream. As an example for various hormone amyloids, we have studied the endogenous opioid neuropeptide β-endorphin in one of its fibril forms. We have achieved the sequential assignment of the chemical shifts of the backbone and side-chain heavy atoms of the fibril. The secondary chemical shift analysis revealed that the β-endorphin peptide adopts three β-strands in its fibril state. This finding fosters the amyloid nature of a hormone at the atomic level.